Evidence map›Paper›PMID 36929192›Full record

ArticleApplied microbiology and biotechnology2023

Characterization of three succinyl-CoA acyltransferases involved in polyketide chain assembly.

Lilu Liu, Wenzhao Wang, Meng Chen, Yuwei Zhang, Huijin Mao, Dacheng Wang, Yihua Chen, Pengwei Li

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Lilu Liu *State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Wenzhao Wang *State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Meng ChenState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yuwei ZhangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Huijin MaoState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Dacheng WangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yihua ChenState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Pengwei LiState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. lipw@im.ac.cn.ORCID http://orcid.org/0000-0003-3288-9214
Chinese Academy of Sciences · CN

Funding

Biological Resources Program, CAS KFJ-BRP-009Central Asian Center of Drug Discovery and Development, Chinese Academy of Sciences CAM202202Ministry of Science and Technology of the People's Republic of China 2018YFA0901600Natural Science Foundation of China 32000042Natural Science Foundation of China 32025002Youth Innovation Promotion Association of the Chinese Academy of Sciences No. 2023097
6 · The paper itself

Abstract

Polyketides are a class of natural products with astonishing structural diversities, fascinating biological activities, and a versatile of applications. In polyketides biosynthesis, acyltransferases (ATs) are the 'gatekeeping' enzymes selecting the specific CoA-activated acyl groups as building blocks and transferring them onto the phosphopantetheine arm of acyl carrier proteins (ACPs) to enable the following condensation reactions to assemble the polyketide chain. Herein, the Art2 protein from aurantinins, a group of the antibacterial polyketides, is characterized in vitro as an AT that can load a CoA-activated succinyl unit onto the first ACP domain of Art17 (ACP

Indexed as

AcyltransferasesPolyketidesAcyl Coenzyme AAnti-Bacterial AgentsPolyketide SynthasesAcyl Coenzyme AAcyltransferasesAnti-Bacterial AgentsPolyketidesPolyketide Synthasessuccinyl-coenzyme AAcyltransferaseBiosynthesisPolyketidesSuccinyl-CoA

Identifiers

PMID36929192
OpenAlexW4327679570

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.